Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2234-8.

Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.

Kayalar C, Ord T, Testa MP, Zhong LT, Bredesen DE.

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La Jolla Cancer Research Foundation, CA 92037, USA.

Abstract

Three of the predominant features of apoptosis are internucleosomal DNA fragmentation, plasma membrane bleb formation, and retraction of cell processes. We demonstrate that actin is a substrate for the proapoptotic cysteine protease interleukin 1beta-converting enzyme. Actin cleaved by interleukin 1beta-converting enzyme can neither inhibit DNase I nor polymerize to its filamentous form as effectively as intact actin. These findings suggest a mechanism for the coordination of the proteolytic, endonucleolytic, and morphogenetic aspects of apoptosis.

PMID:: 8700913; [PubMed - indexed for MEDLINE]
PMCID: PMC39941

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Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.

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